Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
news and views 1082 nature structural biology volume 7 number 12 december 2000
 

Summary: news and views
1082 nature structural biology volume 7 number 12 december 2000
Water is essential for life. However, cellu-
lar membranes provide efficient barriers
that impede the free permeation of water,
small solutes and ions. The discovery of
channel proteins that lower the energy
barrier for the translocation of water and
small solutes across the lipid bilayer pre-
sented a puzzle as to how these channels
achieve selectivity. The answer begins to
emerge as the teams led by Fujiyoshi and
Stroud report the atomic models of the
mammalian water channel AQP1 (ref. 1)
and the bacterial glycerol facilitator
GlpF2 in recent issues of Nature and
Science, respectively. Not unlike fraternal
twins, the overall structures of these pro-
teins are very similar. This was expected
given that both proteins belong to sub-

  

Source: Akabas, Myles - Department of Physiology and Biophysics, Albert Einstein College of Medicine, Yeshiva University

 

Collections: Biology and Medicine